WordNet
- of or relating to a focus; "focal length"
- having or localized centrally at a focus; "focal point"; "focal infection"
- a fibrous band of scar tissue that binds together normally separate anatomical structures
- abnormal union of bodily tissues; most common in the abdomen
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
- an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
- an amino acid found in most proteins; a precursor of several hormones
PrepTutorEJDIC
- 焦点の
- 粘着,付着
- 蛋白(たんばく)質
UpToDate Contents
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- 1. 慢性骨髄性白血病の細胞生物学および分子生物学 cellular and molecular biology of chronic myeloid leukemia
- 2. リウマチ性疾患におけるサイトカインネットワーク：治療の意味 cytokine networks in rheumatic diseases implications for therapy
- 3. 急性骨髄性白血病の予後 prognosis of acute myeloid leukemia
- 4. 子癇前症：病因 preeclampsia pathogenesis
- 5. インスリン受容体の構造および機能 structure and function of the insulin receptor
English Journal
- Interaction of membrane/lipid rafts with the cytoskeleton: Impact on signaling and function: Membrane/lipid rafts, mediators of cytoskeletal arrangement and cell signaling.
- Head BP1, Patel HH1, Insel PA2.Author information 1VA San Diego Healthcare System, 3350 La Jolla Village Drive, San Diego, CA 92161, USA; Department of Anesthesiology, University of California, San Diego, La Jolla, CA 92093, USA.2Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093, USA; Department of Medicine, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: pinsel@ucsd.edu.AbstractThe plasma membrane in eukaryotic cells contains microdomains that are enriched in certain glycosphingolipids, gangliosides, and sterols (such as cholesterol) to form membrane/lipid rafts (MLR). These regions exist as caveolae, morphologically observable flask-like invaginations, or as a less easily detectable planar form. MLR are scaffolds for many molecular entities, including signaling receptors and ion channels that communicate extracellular stimuli to the intracellular milieu. Much evidence indicates that this organization and/or the clustering of MLR into more active signaling platforms depends upon interactions with and dynamic rearrangement of the cytoskeleton. Several cytoskeletal components and binding partners, as well as enzymes that regulate the cytoskeleton, localize to MLR and help regulate lateral diffusion of membrane proteins and lipids in response to extracellular events (e.g., receptor activation, shear stress, electrical conductance, and nutrient demand). MLR regulate cellular polarity, adherence to the extracellular matrix, signaling events (including ones that affect growth and migration), and are sites of cellular entry of certain pathogens, toxins and nanoparticles. The dynamic interaction between MLR and the underlying cytoskeleton thus regulates many facets of the function of eukaryotic cells and their adaptation to changing environments. Here, we review general features of MLR and caveolae and their role in several aspects of cellular function, including polarity of endothelial and epithelial cells, cell migration, mechanotransduction, lymphocyte activation, neuronal growth and signaling, and a variety of disease settings. This article is part of a Special Issue entitled: Reciprocal influences between cell cytoskeleton and membrane channels, receptors and transporters. Guest Editor: Jean Claude Hervé.
- Biochimica et biophysica acta.Biochim Biophys Acta.2014 Feb;1838(2):532-45. doi: 10.1016/j.bbamem.2013.07.018. Epub 2013 Jul 27.
- The plasma membrane in eukaryotic cells contains microdomains that are enriched in certain glycosphingolipids, gangliosides, and sterols (such as cholesterol) to form membrane/lipid rafts (MLR). These regions exist as caveolae, morphologically observable flask-like invaginations, or as a less easily
- PMID 23899502
- STRIPAK complexes: Structure, biological function, and involvement in human diseases.
- Hwang J1, Pallas DC2.Author information 1Department of Biochemistry and Winship Cancer Institute, and Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA. Electronic address: jhwang8231@gmail.com.2Department of Biochemistry and Winship Cancer Institute, and Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA. Electronic address: dpallas@emory.edu.AbstractThe mammalian striatin family consists of three proteins, striatin, S/G2 nuclear autoantigen, and zinedin. Striatin family members have no intrinsic catalytic activity, but rather function as scaffolding proteins. Remarkably, they organize multiple diverse, large signaling complexes that participate in a variety of cellular processes. Moreover, they appear to be regulatory/targeting subunits for the major eukaryotic serine/threonine protein phosphatase 2A. In addition, striatin family members associate with germinal center kinase III kinases as well as other novel components, earning these assemblies the name striatin-interacting phosphatase and kinase (STRIPAK) complexes. Recently, there has been a great increase in functional and mechanistic studies aimed at identifying and understanding the roles of STRIPAK and STRIPAK-like complexes in cellular processes of multiple organisms. These studies have identified novel STRIPAK and STRIPAK-like complexes and have explored their roles in specific signaling pathways. Together, the results of these studies have sparked increased interest in striatin family complexes because they have revealed roles in signaling, cell cycle control, apoptosis, vesicular trafficking, Golgi assembly, cell polarity, cell migration, neural and vascular development, and cardiac function. Moreover, STRIPAK complexes have been connected to clinical conditions, including cardiac disease, diabetes, autism, and cerebral cavernous malformation. In this review, we discuss the expression, localization, and protein domain structure of striatin family members. Then we consider the diverse complexes these proteins and their homologs form in various organisms, emphasizing what is known regarding function and regulation. Finally, we explore possible roles of striatin family complexes in disease, especially cerebral cavernous malformation.
- The international journal of biochemistry & cell biology.Int J Biochem Cell Biol.2014 Feb;47:118-48. doi: 10.1016/j.biocel.2013.11.021. Epub 2013 Dec 11.
- The mammalian striatin family consists of three proteins, striatin, S/G2 nuclear autoantigen, and zinedin. Striatin family members have no intrinsic catalytic activity, but rather function as scaffolding proteins. Remarkably, they organize multiple diverse, large signaling complexes that participate
- PMID 24333164
- Grb2 Promotes Integrin-Induced Focal Adhesion Kinase (FAK) Autophosphorylation and Directs the Phosphorylation of Protein Tyrosine Phosphatase α by the Src-FAK Kinase Complex.
- Cheng SY, Sun G, Schlaepfer DD, Pallen CJ.Author information Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, British Columbia, Canada.AbstractThe integrin-activated Src-focal adhesion kinase (FAK) kinase complex phosphorylates PTPα at Tyr789, initiating PTPα-mediated signaling that promotes cell migration. Recruitment of the BCAR3-Cas complex by PTPα-phospho-Tyr789 at focal adhesions is one mechanism of PTPα signaling. The adaptor protein Grb2 is also recruited by PTPα-phospho-Tyr789, although the role of the PTPα-Grb2 complex in integrin signaling is unknown. We show that silencing Grb2 expression in fibroblasts abolishes PTPα-Tyr789 phosphorylation and that this is due to two unexpected actions of Grb2. First, Grb2 promotes integrin-induced autophosphorylation of FAK-Tyr397. This is impaired in Grb2-depleted cells and prohibits FAK activation and formation of the Src-FAK complex. Grb2-depleted cells contain less paxillin, and paxillin overexpression rescues FAK-Tyr397 phosphorylation, suggesting that the FAK-activating action of Grb2 involves paxillin. A second distinct role for Grb2 in PTPα-Tyr789 phosphorylation involves Grb2-mediated coupling of Src-FAK and PTPα. This requires two phosphosites, FAK-Tyr925 and PTPα-Tyr789, for Grb2-Src homology 2 (SH2) binding. We propose that a Grb2 dimer links FAK and PTPα, and this positions active Src-FAK in proximity with other, perhaps integrin-clustered, molecules of PTPα to enable maximal PTPα-Tyr789 phosphorylation. These findings identify Grb2 as a new FAK activator and reveal its essential role in coordinating PTPα tyrosine phosphorylation to enable downstream integrin signaling and migration.
- Molecular and cellular biology.Mol Cell Biol.2014 Feb;34(3):348-61. doi: 10.1128/MCB.00825-13. Epub 2013 Nov 18.
- The integrin-activated Src-focal adhesion kinase (FAK) kinase complex phosphorylates PTPα at Tyr789, initiating PTPα-mediated signaling that promotes cell migration. Recruitment of the BCAR3-Cas complex by PTPα-phospho-Tyr789 at focal adhesions is one mechanism of PTPα signaling. The adaptor pro
- PMID 24248601
Japanese Journal
- Hypertension Promotes Phosphorylation of Focal Adhesion Kinase and Proline-Rich Tyrosine Kinase 2 in Rats: Implication for the Pathogenesis of Hypertensive Vascular Disease
- Sugimura Koichiro,Fukumoto Yoshihiro,Nawata Jun,Wang Huan,Onoue Noriko,Tada Tomohiro,Shirato Kunio,Shimokawa Hiroaki
- The Tohoku Journal of Experimental Medicine 222(3), 201-210, 2010
- … Atherosclerosis is initiated by adhesion and infiltration of inflammatory leukocytes into the intima, where non-receptor protein tyrosine kinases, such as focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK2), play important roles as intracellular messengers of mechanical and biochemical signals. …
- NAID 130004459865
- Tyrosine phosphorylation of the CrkII adaptor protein modulates cell migration
- TAKINO T.
- Journal of Cell Science 116(15), 3145-3155, 2003-08
- … CrkII belongs to a family of adaptor proteins that become tyrosine phosphorylated after various stimuli. … We examined the role of CrkII tyrosine phosphorylation in fibronectin-induced cell migration. … Overexpression of CrkII inhibited dephosphorylation of focal adhesion components such as p130 Crk-associated substrate (p130cas) and paxillin by protein tyrosine phosphatase 1B (PTP1B). …
- NAID 80016110981
- Nuclear Translocation of Cell Adhesion Kinase .BETA./Proline-rich Tyrosine Kinase 2.
- Aoto Hiroshi,Sasaki Hiroko,Ishino Masaho,Sasaki Terukatsu
- Cell Structure and Function 27(1), 47-61, 2002
- … Cell adhesion kinase β (CAKβ/PYK2) is a protein-tyrosine kinase of the focal adhesion kinase (FAK) family. … Whereas FAK predominantly localizes at focal adhesions, CAK β localizes at the perinuclear region in fibroblasts. …
- NAID 130004137433
Related Links
- Focal adhesion kinase (FAK) is a nonrecepor protein tyrosine kinase that is associated with focal adhesions and regulates cell spreading and migration. It is a ... Splice Variants/Polymorphisms Chicken fibroblasts and vascular ...
- Focal adhesion kinase (pp125FAK), a protein tyrosine kinase, has recently been suggested to regulate aspects of signalling induced by integrins and by certain g ... 35. S. Tanaka, T. Morishita, Y. Hashimoto, S. Hattori, S ...
Related Pictures
★リンクテーブル★
| リンク元 | 「接着斑キナーゼ」「FAK」「focal adhesion kinase」「フォーカルアドヒージョンキナーゼ」 |
| 関連記事 | 「focal」「adhesion」「focal adhesion」「kinase」 |
「接着斑キナーゼ」
- 英
- focal adhesion kinase、focal adhesion protein-tyrosine kinase、FAK
- 関
- 局所接着キナーゼ、焦点接着キナーゼ、フォーカルアドヒージョンキナーゼ
「FAK」
「focal adhesion kinase」
「フォーカルアドヒージョンキナーゼ」
「focal」
- adj.
- 焦点の、焦点を通る
- (病変が)限局性の、局所の、病巣の、巣状の
- 関
- circumscribed、definite、focal point、focally、foci、focus、local、localized、locally、nidal、nidus、topical、topically
「adhesion」
- n